The work proposed for the coming year will continue the oxygen-17 NMR studies of peptides conformation and motional dynamics. A fundamental theoretical and experimental understanding of the effects of hydrogen bonding, weak interactions, substituents, and various physio-chemical perturbations on the oxygen-17 NMR parameters in amides, amino acids, aromatic acyl compounds and low molecular weight peptides has been established. Future studies will include the application of these results to metal ion-peptide interactions, quantifying the hydrogen bonding force in peptide systems via the oxygen-17 NMR parameters, establishing the utility of this method in elucidating conformational changes in peptides, processing information regarding inter and intramolecular modes of motion, and extending this work to higher molecular weight physiologically active peptides.